BMP-2 expression is linked to cancer invasion and. BMPs are synthesized as inactive proteins of variable length. The precursor BMP-2 and BMP-4 proteins are proteolytically cleaved, producing mature C-terminal proteins of a little more than 100 residues. BMP-2 and BMP-4 interact with the same binding sites: mature BMP-2 and BMP-4 protein signaling is mediated by transmembrane serine/threonine kinases called type IA, IB, and type II receptors. The receptor phosphorylates cytoplasmic targets, which include the Smad family of proteins. In addition, the same molecules including noggin, chordin, DAN, gremlin, and Cerberus 1 homolog, inhibit both BMP-2 and BMP-4, thereby preventing their ability to bind to the receptors. While BMP expression has been noted in a few cancers, such as sarcomas and in pancreatic cancer and in cancer cell lines, the inhibition of BMP-2 activity and/or BMP-4 activity as a potential cancer treatment has never been mentioned. BMP-2 expression is linked to cancer invasion and growth and inhibiting BMP-2 activity reduces the size of cancerous tumors in nude mice and down regulates the expression of VEGF and sonic hedgehog in lung cancer cell lines. The present technology provides amino acid sequence of inhibitors to BMP-2 and BMP-4 and the receptor site for BMP-2 and BMP-4 antibodies.
- Allows for early detection of metastases and treatment
- Technology provides novel sequences and receptor sites
Intellectual Property & Development Status:
United States patent number US 7,473,561 granted on January 6, 2009